AFfirm™ SIAH2 Mouse Monoclonal Antibody - #BF8278
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
E3 ubiquitin-protein ligase Siah2;hSiah2;Seven in absentia homolog 2;Siah E3 ubiquitin protein ligase 2;Siah-2;siah2;SIAH2_HUMAN;Ubiquitin Ligase Siah2;
Immunogens
- O43255 SIAH2_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSRPSSTGPSANKPCSKQPPPQPQHTPSPAAPPAAATISAAGPGSSAVPAAAAVISGPGGGGGAGPVSPQHHELTSLFECPVCFDYVLPPILQCQAGHLVCNQCRQKLSCCPTCRGALTPSIRNLAMEKVASAVLFPCKYATTGCSLTLHHTEKPEHEDICEYRPYSCPCPGASCKWQGSLEAVMSHLMHAHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYEGHQQFFAIVLLIGTRKQAENFAYRLELNGNRRRLTWEATPRSIHDGVAAAIMNSDCLVFDTAIAHLFADNGNLGINVTISTCCP
PTMs - O43255 As Substrate
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| S2 | Phosphorylation | Uniprot | |
| S6 | Phosphorylation | Uniprot | |
| T7 | Phosphorylation | Uniprot | |
| S10 | Phosphorylation | Uniprot | |
| K13 | Ubiquitination | Uniprot | |
| S16 | Phosphorylation | Q92630 (DYRK2) | Uniprot |
| T26 | Phosphorylation | O96017 (CHEK2) , Q92630 (DYRK2) , Q9H2X6 (HIPK2) | Uniprot |
| S28 | Phosphorylation | Q16539 (MAPK14) , Q92630 (DYRK2) , O96017 (CHEK2) , Q9H2X6 (HIPK2) | Uniprot |
| S68 | Phosphorylation | Q9H2X6 (HIPK2) , Q92630 (DYRK2) , O96017 (CHEK2) | Uniprot |
| K107 | Ubiquitination | Uniprot | |
| T119 | Phosphorylation | O96017 (CHEK2) , Q92630 (DYRK2) | Uniprot |
| S132 | Phosphorylation | Uniprot | |
| S167 | Phosphorylation | Uniprot | |
| T254 | Phosphorylation | Uniprot | |
| K256 | Ubiquitination | Uniprot |
Research Backgrounds
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia. It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not. Promotes monoubiquitination of SNCA. Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation. Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance.
Phosphorylated at Ser-28 by MAPK14, which mediates the degradation by the proteasome of EGLN3 (By similarity). Phosphorylated at Ser-28 by DYRK2; this increases the ubiquitin ligase activity and promotes degradation of EGLN3.
Cytoplasm. Nucleus.
Note: Predominantly cytoplasmic. Partially nuclear.
Widely expressed at low level.
Homodimer. Interacts with UBE2E2. Interacts with PEG3 (By similarity). Interacts with VAV1, without mediating its ubiquitin-mediated degradation. Interacts with CACYBP/SIP. Probable component of some large E3 complex possibly composed of UBE2D1, SIAH2, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with PEG10, which may inhibit its activity. Interacts with EGLN2 and SNCAIP. Interacts with DYRK2. Interacts with NR1D1 and NR1D2. Interacts with DCC.
The RING-type zinc finger domain is essential for ubiquitin ligase activity.
The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family.
Belongs to the SINA (Seven in absentia) family.
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